5.3.4.1: protein disulfide-isomerase
This is an abbreviated version!
For detailed information about protein disulfide-isomerase, go to the full flat file.
Word Map on EC 5.3.4.1
-
5.3.4.1
-
collagen
-
laminin
-
integrins
-
endothelial
-
actin
-
fibrosis
-
adhesive
-
basement
-
mesenchymal
-
vessel
-
fiber
-
metastasis
-
proteoglycans
-
vitronectin
-
fibrinogen
-
matrices
-
nephropathy
-
albumin
-
gelatin
-
interstitial
-
mesangial
-
platelet
-
monolayer
-
cytoskeleton
-
glomerular
-
rgd
-
vimentin
-
e-cadherin
-
cell-cell
-
adhesions
-
zeta
-
myofibroblasts
-
willebrand
-
epithelial-mesenchymal
-
factor-beta
-
fak
-
fibrin
-
metalloproteinases
-
preterm
-
dish
-
biomaterials
-
procollagens
-
heparan
-
alpha-smooth
-
dermal
-
tgf-beta
-
plasminogen
-
fibrillar
-
drug development
-
heparin-binding
-
synthesis
-
thrombospondin
-
medicine
-
industry
-
diagnostics
-
pharmacology
-
biotechnology
-
analysis
- 5.3.4.1
- collagen
- laminin
- integrins
- endothelial
- actin
- fibrosis
-
adhesive
-
basement
- mesenchymal
- vessel
- fiber
- metastasis
- proteoglycans
- vitronectin
- fibrinogen
- matrices
- nephropathy
- albumin
- gelatin
-
interstitial
-
mesangial
- platelet
- monolayer
- cytoskeleton
- glomerular
- rgd
- vimentin
- e-cadherin
-
cell-cell
- adhesions
- zeta
- myofibroblasts
- willebrand
-
epithelial-mesenchymal
- factor-beta
- fak
- fibrin
- metalloproteinases
-
preterm
-
dish
-
biomaterials
- procollagens
- heparan
-
alpha-smooth
- dermal
- tgf-beta
- plasminogen
-
fibrillar
- drug development
-
heparin-binding
- synthesis
- thrombospondin
- medicine
- industry
- diagnostics
- pharmacology
- biotechnology
- analysis
Reaction
catalyses the rearrangement of -S-S- bonds in proteins =
Synonyms
5'-MD, 58 kDa glucose regulated protein, 58 kDa microsomal protein, AGR2, anterior gradient homolog 2, BPA-binding protein, CaBP1, CaBP2, Cellular thyroid hormone binding protein, cotyledon-specific chloroplast biogenesis factor CYO1, CYO1, DbsG, disulfide bond isomerase, disulfide bond-forming enzyme, Disulfide interchange enzyme, disulfide isomerase, Disulfide isomerase ER-60, disulfide-bond isomerase, dithiol-disulfide isomerase, Dsb, DsbA, DsbB, DsbC, DsbD, DsbG, ECaSt/PDI, endoplasmic reticulum protein EUG1, Eps1p, ER protein 57, ER58, ER60, ERcalcistorin/protein-disulfide isomerase, ERdj5, Ero1, Erp, ERP-57, ERp-72 homolog, ERp18, ERp27, ERp28, ERp44, Erp46, ERp5, ERp57, ERP59, ERP60, ERp72, Eug1p, fibronectin, gPDI-1, gPDI-2, gPDI-3, HIP-70, HlPDI-1, HlPDI-2, HlPDI-3, Iodothyronine 5'-monodeiodinase, More, Mpd1p, Mpd2p, multifunctional protein disulfide isomerase, ncgl2478, P5, P55, P58, pancreas-specific protein disulfide isomerase, PDI, PDI A4, PDI I, PDI II, pdi-15, PDI-1a, pdi-40, pdi-47, pdi-52, PDI-A, PDI-M, PDI-P5, PDI-related protein, PDI1, PDI11, PDI2, PDI7, PDI8, PDIA1, PDIA2, PDIA3, PDIA4, PDIA6, PDIL-1, PDIL-2, PDIL1-1, PDIL1;1, PDIL1Aalpha, PDIL1B, PDIL2, PDIL2-3, PDIL3A, PDIL4D, PDIL5A, PDILT, PDIp, PDIr, protein disulfide isomerase, protein disulfide isomerase 1, protein disulfide isomerase 2, protein disulfide isomerase 3, protein disulfide isomerase A1, protein disulfide isomerase A3, protein disulfide isomerase A5, protein disulfide isomerase A6, protein disulfide isomerase associated 3, Protein disulfide isomerase P5, protein disulfide isomerase-1, protein disulfide isomerase-11, protein disulfide isomerase-2, protein disulfide isomerase-3, protein disulfide isomerase-8, protein disulfide isomerase-like protein of the testis, protein disulfide isomerase-P5, protein disulfide isomerase-related chaperone Wind, Protein disulfide isomerase-related protein, protein disulfide oxidoreductase, protein disulfide reductase/isomerase, protein disulfide-isomerase A4, Protein disulphide isomerase, Protein ERp-72, protein-disulfide isomerase, R-cognin, RB60, Rearrangease, Reduced ribonuclease reactivating enzyme, Retina cognin, S-S rearrangase, SSO0192, SsPDO, thiol-disulfide oxidoreductase, thiol-protein oxidoreductase, thioredoxin domain-containing protein 5, Thyroid hormone-binding protein, Thyroxine deiodinase, TXNDC5, yPDI
ECTree
5.3.4.1 protein disulfide-isomeraseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 5.3.4.1 - protein disulfide-isomerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Agp mutant
?
-
folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond
-
-
?
alpha-globulin
?
PDIL1-1 facilitates the oxidative folding of alpha-globulin
-
-
?
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
cholera toxin
?
-
reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit
-
-
?
citrate synthase
stabilized citrate synthase
-
DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
-
?
conotoxins sTx3.1
?
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
conotoxins tx3a
?
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
creatine kinase
?
-
refolding of creatine kinase, creatine kinase substrate is denatured by 3 M guanidine-HCl, catalysis of creatine kinase refolding by PDI involves disulfide cross-link and dimer to tetramer switch, PDI suppresses aggregation of denatured inactive casein kinase
-
-
?
degenerated RNase type III
?
refolding of degenerated RNase type III, bovine pancreatic substrate, recombinant GST-tagged PDI, the coupled-assay method involves reduction of insulin in presence of DTT
-
-
?
denatured D-glceraldehyde-3-phosphate dehydrogenase
refolded D-glceraldehyde-3-phosphate dehydrogenase
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
-
chaperone activity of PDI
-
?
denatured eclosion hormone
active eclosion hormon
-
PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone
-
?
denatured lysozyme
?
-
PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
-
-
?
denatured rhodanese
refolded rhodanese
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
-
PDI I and PDI II foster heterodimer formation between E proteins, i.e. basic-loop-helix proteins of the E2A gene products, by a redox mechanism
-
?
envelope glycoprotein 120
envelope glycoprotein 120
-
i.e. human immunodeficiency virus gp120
-
?
folded cholera toxin
unfolded cholera toxin
-
PDI binds in the reduced state to the A chain of cholera toxin, in the oxidized state it releases it, PDI may be involved in the retrograde protein transport into the cytosol
-
?
glycoprotein 120
glycoprotein 120
-
PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120
-
?
GSSG
GSH
-
disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced
-
-
?
insulin + DTT
?
bovine substrate, reductase activity with DTT
-
-
?
Insulin-(SS) + dithiothreitol
Insulin-(SH)2 + oxidized dithiothreitol
-
-
-
?
integrin subunit alpha11
?
-
the enzyme activates integrin subunit alpha11
-
-
?
kalata B1
?
-
and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates
-
-
?
lactate dehydrogenase
?
-
reactivation of self-aggregated denatured lactate dehydrogenase, guanidine HCl-denatured LDH, chaperone activity, both recombinant wild-type PDI and mutant abb'a' interact with self-aggregated lactate dehydrogenase enhancing LDH reactivation and reducing aggregation
-
-
?
luciferase
stabilized luciferase
-
DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
-
?
lysozyme
?
PDI exhibits both chaperone and antichaperone activities when catalyzing the refolding of reduced/denatured lysozyme in HEPES buffer, effect of macromolecular crowding on the PDI-catalyzed folding, overview
-
-
?
lysozyme
aggregated lysozyme
-
PDI has antichaperone activity facilitating protein aggregation
-
?
NADP malate dehydrogenase
?
-
substrate for isoform PDI-M only
-
-
?
neuronal nitric oxide synthase
?
-
the enzyme catalyzes neuronal nitric oxide synthase dimerization
-
-
?
oxidized insulin + dithiothreitol
reduced insulin
gPDI-2, low activity with gPDI-3, no activity with gPDI-1
-
?
oxidoreductase Ero1
?
-
disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT
-
-
?
phytase
?
-
folding of phytase, i.e. AppA, substrate from Escherichia coli, contains 3 consecutive and 1 nonconsecutive disulfide bonds, DsbC, no activity of DsbC with an AppA mutant C155S/C430S lacking the nonconsecutive disulfide bond
-
-
?
Pipe
?
-
processing and targeting of Pipe, Pipe is an essential Golgi transmembrane-O-sulfotransferase, protein disulfide isomerase-related chaperone Wind is required for processing and correct targeting of the substrate, mapping of multiple substrate binding sites in Pipe, one enzyme site in vicinity of an exposed cluster of tyrosine residues within the thioredoxin fold domain is essential for activity, a second enzyme site in the enzyme's D-domain is also necessary for processing activity, but competitive to the thioredoxin fold domain residue, overview
-
-
?
reduced bovine pancreatic trypsin inhibitor
oxidized bovine pancreatic trypsin inhibitor
gPDI-2, no cativity with gPDI-1 and gPDI-3
-
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
-
-
-
-
?
reduced ribonuclease
?
-
refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
-
-
?
reduced ribonuclease A
denatured ribonuclease A
-
-
-
?
riboflavin binding protein
?
-
protein disulfide isomerase and quiescin-sulfhydryl oxidase cooperate in vitro to generate native pairings in substrates ribonuclease A, with four disulfide bonds and 105 disulfide isomers of the fully oxidized protein, and avian riboflavin binding protein, with nine disulfide bonds and more than 34 million corresponding disulfide pairings. The isomerase is not a significant substrate of quiescin-sulfhydryl oxidase. Both reduced RNase and riboflavin binding protein can be efficiently refolded in an aerobic solution containing micromolar concentrations of reduced PDI and nanomolar levels of quiescin-sulfhydryl oxidase without any added oxidized PDI or glutathione redox buffer. In the absence of either quiescin-sulfhydryl oxidase or redox buffer, the fastest refolding of riboflavin binding protein is accomplished with excess reduced PDI and just enough oxidized PDI to generate nine disulfides in the protein client
-
-
?
ribonuclease A
?
-
protein disulfide isomerase and quiescin-sulfhydryl oxidase cooperate in vitro to generate native pairings in ribonuclease A, with four disulfide bonds and 105 disulfide isomers of the fully oxidized protein, and avian riboflavin binding protein, with nine disulfide bonds and more than 34 million corresponding disulfide pairings. The isomerase is not a significant substrate of quiescin-sulfhydryl oxidase. Both reduced RNase and riboflavin binding protein can be efficiently refolded in an aerobic solution containing micromolar concentrations of reduced PDI and nanomolar levels of quiescin-sulfhydryl oxidase without any added oxidized PDI or glutathione redox buffer
-
-
?
ricin
?
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
ricin A-chain immunotoxins
?
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
RNase B
?
the ability of the ERp57-calnexin complex to mediate folding of 3H-labeled RNase B is completely dependent on a functional interaction between ERp57 and calnexin, overview
-
-
?
thrombospondin-1 + alpha-thrombin + antithrombin III
thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III
-
PDI catalyzes formation of disulfide linked complexes of thrombospondin
-
?
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
-
PDI at a molar ratio to acidic phospholipase A2 of 0.1 increases the reactivation of reduced and denatured acidic phospholipase A2 from 4% to 15%
-
?
unfolded bovine pancreatic ribonuclease A + oxidized glutathione
refolded bovine pancreatic ribonuclease A + reduced glutathione
-
oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI
-
?
unfolded bovine pancreatic trypsin inhibitor
folded bovine pancreatic trypsin inhibitor
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor + oxidized glutathione
-
oxidative refolding of denatured bovine pancreatic trypsin inhibitor
-
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
-
-
-
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
-
-
-
?
unfolded lysozyme
refolded lysozyme
-
oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer
-
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
-
maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
-
?
unfolded pro-carboxypeptidase Y
refolded pro-carboxypeptidase Y
-
-
-
?
unfolded proinsulin
refolded proinsulin
-
PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity
-
?
unfolded RNase A + reduced glutathione
refolded RNase A + oxidized glutathione
-
-
-
?
unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol
refolded bovine pancreatic ribonuclease A + reduced dithiothreitol
-
oxidative folding of RNase A
-
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
-
PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
-
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
-
-
?
estrogen receptor alpha
?
-
i.e. ERalpha, PDI plays a critical role in estrogen responsiveness by functioning as a molecular chaperone and assisting the receptor in differentially regulating target gene expression, PDI alters estrogen-mediated transactivation, overview, PDI enhances ERalpha-DNA interactions in presence of an oxidizing agent
-
-
?
estrogen receptor alpha
?
-
i.e. ERalpha, PDI colocalizes with ERalpha in MCF-7 nuclei, alters ERalpha conformation, enhances the ERalpha-estrogen response element interaction in the absence and presence of an oxidizing agent, influences the ability of ERalpha to mediate changes in gene expression, and associates with promoter regions of two endogenous estrogen-responsive genes, overview
-
-
?
insulin
?
recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin
-
-
?
insulin
?
-
reduction of insulin, turbidometry assay including glutathione reduction and alkylation of 4-acetamido-4'-maleimidyl-stilbene-2,2'-disulfonate, as well as treatment with DTT and iodoacetamide or iodoacetate for subsequent insulin reduction, isomerase activity, overview
-
-
?
insulin
?
-
disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
-
-
?
NRCSQGSCWN
?
-
disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG
-
-
?
Proteins
?
-
facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
-
-
?
Proteins
?
-
catalyzes disulfide cleavage in membrane-bound diphtheria toxin or the membrane-bound conjugate, iodotyramine conjugated with poly(D-Lys) via a 3,3'-dithiobis(propionic acid) spacer
-
-
?
Proteins
?
-
enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
may play a role in retaining prolyl 4-hydroxylase in its native conformation
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
when present in large stoichiometric excess relative to an unfolded protein substrate, the enzyme can exhibit chaperone activity, inhibiting aggregation and increasing the recovery of native protein
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
?
Proteins
?
-
involved in the assembly of wheat storage proteins within the endoplasmic reticulum
-
-
?
Proteins
?
-
plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding and activation of human carbonic anhydrase IV, GSSG promotes the activation
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked bovine pancreatic ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked Bowman Birk soybean trypsin
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked lysozyme
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled lysosyme
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
eduction of insulin and oxidative folding of ribonuclease A
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
rhodanese
?
-
the protein substrate is devoid of disulfide bonds, chaperone activity
-
-
?
rhodanese
?
-
prevention of rhodanese degeneration, chaperone activity
-
-
?
rhodanese
?
-
prevention of rhodanese degeneration, chaperone activity
-
-
?
ribonuclease
?
-
refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG
-
-
?
RNase
?
-
refolding of RNase, renaturation of reduced bovine pancreatic RNase
-
-
?
RNase
?
-
refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity
-
-
?
RNase A
?
-
reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
-
-
?
RNase A
?
PDI catalyzes the refolding of denatured bovine RNase A. The protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, overview
-
-
?
RNase A
?
-
reduced and denatured substrate, oxidase/isomerase activity on the refolding of the substrate
-
-
?
RNase A + DTT
?
the enzyme contains a WCGHCK active site
-
-
?
RNase A + DTT
?
the enzyme contains a WCGHCQ active site
-
-
?
scrambled RNAse A
?
the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
-
-
?
scrambled RNAse A
?
the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
-
-
?
tissue factor
?
-
PDI switches tissue factor from coagulation to signaling by targeting the allosteric Cys186-Cys209 disulfide, the tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity, the chaperone activity is sufficient, PDI enhances factor VIIa-dependent substrate factor X activation 5-10fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys186 or Cys209, PDI has no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover, overview
-
-
?
tissue factor
?
-
recombinant wild-type and mutant TFs expressed in Escherichia coli, PDI is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, PDI facilitates ternary complex formation and substrate Turnover, overview
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded RNase
refolded RNase
PDI is a multifunctional enzyme that acts as a subunit in prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding
-
?
unfolded RNase A
refolded RNase A
-
all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity
-
?
unfolded RNase A
refolded RNase A
-
PDI binds to DNA and may be involved in DNA-nuclear matrix anchoring
-
?
unfolded RNase A
refolded RNase A
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
-
PDI functions in a plasma environment
-
?
unfolded RNase A
refolded RNase A
-
reduced and denatured bovine pancreatic RNase A, glutathione redox buffer, PDI catalyzes the entire RNase A folding by enhancing the formation and reduction of mixed disulfides with glutathione and the formation of intramolecular disulfides
-
?
unfolded RNase A
refolded RNase A
-
tyrosine and tryptophane residues in peptides are the recognition motifs for their binding
-
?
additional information
?
-
PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
-
-
?
additional information
?
-
-
PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
-
-
?
additional information
?
-
the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
-
-
?
additional information
?
-
-
the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
-
-
?
additional information
?
-
-
the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
-
-
?
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
?
additional information
?
-
-
the enzyme has oxidative folding activity
-
-
?
additional information
?
-
-
the enzyme may be significant in the action of triiodothyronine towards the target cells
-
-
?
additional information
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition
-
-
?
additional information
?
-
-
PDI is a better thiol oxidant than a disulfide protein reductant
-
-
?
additional information
?
-
-
the enzyme shows disulfide reduction and chaperone activities and contains a WCGHC active site, overview, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
-
-
?
additional information
?
-
-
PDI enhances factor X activation by factor VIIa soluble tissue factor in a dose-dependent manner. The inclusion of annexin V or detergent abolishes the stimulation effect. The presence of 25 nM bovine PDI lowers the apparent Km of factor VIIa for factor X from far above 0.01 mM to 0.001-0.002 mM
-
-
?
additional information
?
-
-
PDI is able to renature reduced-denatured RNase. Plasma transglutaminase-coagulation factor XIII, FXIII, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit
-
-
?
additional information
?
-
-
PDI is able to renature reduced-denatured bovine pancreas RNase A. Plasma transglutaminase-coagulation factor XIII, FXIII, a plasmatic pro-transglutaminase, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit. Both FXIII and tissue transglutaminase exhibit PDI activity sdespite the fact that they lack either the essential amino acid sequence, Cys-X-X-Cys, for PDI activity or its related sequences, Cys-Leu-His-Ser or Cys-Ile-His-Ser, which have been reported to impart such activity, overview
-
-
?
additional information
?
-
-
PDI catalyzes the isomerization of disulfide bonds on misfolded proteins
-
-
?
additional information
?
-
-
study on the interaction of disulfide dyes 2-[(2,4-dinitrophenyl)amino]-3-sulfanylpropanoic acid and 8-[[7,12-diammonio-2-(1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium-8-yl)-6,13-dioxo-5,14-dioxa-9,10-dithia-2-azahexadecan-16-yl](methyl)amino]-1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium
-
-
?
additional information
?
-
-
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, overview, all isozymes are synergistically essential for embryonic development in this nematode
-
-
?
additional information
?
-
-
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme, overview, PDI-2 is required for normal post-embryonic development, all isozymes are synergistically essential for embryonic development in this nematode
-
-
?
additional information
?
-
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
?
additional information
?
-
-
RB60 is involved in the light-regulated translation of the psbA mRNA in the chloroplast of the unicellular alga Chlamydomonas reinhardtii, light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states, overview
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
?
additional information
?
-
-
RB60 binds to RB47 and modulates its activity via redox and phosphorylation events, RB60 attacks the disulfide bond Cys143-Cys259 of RB47, the redox states of the protein redox partners are coupled, overview, recombinant His-tagged RB47 expressed in Escherichia coli
-
-
?
additional information
?
-
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
?
additional information
?
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
the enzyme shows oxidase and isomerase activities, overview
-
-
?
additional information
?
-
-
the enzyme shows oxidase and isomerase activities, overview
-
-
?
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
-
-
-
additional information
?
-
-
the enzyme is involved in diphtheria toxin sensitivity and is required for toxin entry, Chlamydia trachomatis or Chlamydia psittaci, intracellular pathogens of humans, require the enzyme for attachment to mammalian CHO6 cells, host cell invasion is obligatory for survival, growth and pathogenesis, overview
-
-
?
additional information
?
-
-
the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
-
-
?
additional information
?
-
-
the active-site cysteine residues of the functional domains, Trx-domains, are essential for catalysis of disulfide bond formation in polypeptides and proteins, such as the bacterial alkaline phosphatase
-
-
?
additional information
?
-
-
PDI behaves mainly as an oxidase/isomerase and exhibits chaperone-like activity
-
-
?
additional information
?
-
-
DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
-
-
?
additional information
?
-
-
the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in folding periplasmatically excreted proteins
-
-
?
additional information
?
-
-
Cys98 and Cys101 form the reversible disulfide bond in the active site, the enzyme is active in reduced state which is stabilized by hydrogen bond interactions of the active cysteine residues with Thr94 and Thr182
-
-
?
additional information
?
-
-
DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI
-
-
?
additional information
?
-
-
substrate disulfide bonds, overview, the AppA homologue Agp, a periplasmic phosphatase, lacks nonconsecutive disulfide bonds and is no substrate for DsbC
-
-
?
additional information
?
-
-
DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview
-
-
?
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
kinetic cycle of DsbB, thew enzyme uses a tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2, overview
-
-
?
additional information
?
-
-
PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
?
additional information
?
-
-
the enzyme shows disulfide reduction and chaperone activities, it facilitates the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement
-
-
?
additional information
?
-
-
PDI is a subunit of the enzyme prolyl-4-hydroxylase, which catalyzes the formation of 4-hydroxyprolyl residues in nascent collagen-like polypeptides. PDI is also a subunit of a triacylglycerol transfer protein, which facilitates the incorporation of lipids into newly synthesized core lipoproteins within the endoplasmic reticulum. The function of PDI is to maintain the alpha-subunit of this enzyme in an active form
-
-
?
additional information
?
-
-
the enzyme acts as a thyroid-hormone binding protein
-
-
?
additional information
?
-
-
the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview
-
-
?
additional information
?
-
-
PDIS-1 and PDIS-2 show both an oxidative refolding activity of denatured ribonuclease A and a chaperone activity, PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
-
-
?
additional information
?
-
-
enzyme is involved in the proper folding or quality control of storage proteins
-
-
?
additional information
?
-
-
GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
-
-
?
additional information
?
-
-
recombinant GmPDIL-3a and GmPDIL-3b do not function as oxidoreductases or as molecular chaperones in vitro, although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the endoplasmic reticulum. GmPDIL-3a and GmPDIL-3b have no stimulatory effect on the oxidative refolding of RNase A by GmPDIL-1 and GmPDIL-2 when mixed together, further confirming that the functional properties of GmPDIL-3a and GmPDIL-3b are probably unique
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
?
additional information
?
-
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
?
additional information
?
-
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
?
additional information
?
-
-
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
?
additional information
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens
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isomerase activity is assayed using the insulin/glutathione coupled assay
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the four domains a, b, b', and a' show cooperative properties in both isomerase and chaperone functions of PDi
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PDI has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains
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PDIis responsible for correct disulfide bond formation of proteins in the endoplasmic reticulum, it recognize unfolded proteins and can be selective for specific proteins or classes
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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the enzyme mediates rapid delivery of NO signalling into human platelets from the S-nitrosothiol compound S-nitrosoglutathione, NO delivery is blocked by inhibition of PDI, overview
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additional information
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ERp27 is non-catalytic and interacts with ERp57, ERp57 binds ERp27 by the Asp-Glu-Trp-Asp sequence in domain 2, reduced binding to R280A mutant ERp57, overview, it binds DELTA-somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, at its second domain, a significant conformational change in the b'-like domain of ERp27 occurs upon substrate binding, overview
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additional information
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ERp27 is non-catalytic and interacts with ERp57, ERp57 binds ERp27 by the Asp-Glu-Trp-Asp sequence in domain 2, reduced binding to R280A mutant ERp57, overview, it binds DELTA-somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, at its second domain, a significant conformational change in the b'-like domain of ERp27 occurs upon substrate binding, overview
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additional information
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ERp57 interacts with the lectin chaperone calnexin, binding structure, and active site structure, overview
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additional information
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PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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additional information
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the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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additional information
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the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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additional information
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the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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additional information
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the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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additional information
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PDI can function as a high-capacity intracellular 17beta-estradiol-binding protein that increases the concentration and accumulation of 17beta-estradiol in live cells. The intracellular PDI-bound 17beta-estradiol can be released from PDI upon a drop in 17beta-estradiol levels and the released 17beta-estradiol can augment estrogen receptor-mediated transcriptional activity and mitogenic actions in cultured cells. The binding of 17beta-estradiol by PDI also reduces the rate of metabolic disposition of this hormone
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additional information
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protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
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protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
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additional information
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in vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
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presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
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recombinant human PDI does not influence factor X activation by factor VIIa soluble tissue factor
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additional information
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reduced protein disulfide isomerase activates initiator protein tissue factor by isomerzation of a mixed disulfide and a free thiol to an intramolecular disulfide
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the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
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additional information
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the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
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additional information
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PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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additional information
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PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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additional information
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ER protein 57, ERP-57, also known as PDIA3, has disulfide oxidoreductase and isomerase activity. ERP-57 interacts with calnexin, CANX, a chaperone protein and a lectin that binds glycoproteins through a transient oligosaccharide intermediate, thought to prevent a rapid degradation, as well as endoplasmic reticulum retention, of misfolded proteins, overview
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PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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additional information
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PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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additional information
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PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
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additional information
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
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formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo
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formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo
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additional information
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PDI forms mixed disulfides in substrate molecules, substrates are Ero1alpha, clusterin, or PTX3, analysis of PDI substrate specificity, comparison to other members of the protein disulfide isomerase family of oxidoreductases, overview
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additional information
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the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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additional information
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the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
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TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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the enzyme has a single E2-binding site
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PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function
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additional information
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PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
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additional information
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PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
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additional information
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the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
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additional information
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the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
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additional information
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protein disulfide isomerase serves as a subunit of at least two enzymes, the beta-subunit of the enzyme prolyl hydroxylase and an ER triglyceride transferase
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PDILT forms intermolecular disulfide bonds in testis
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PDILT forms intermolecular disulfide bonds, but shows no intramolecular disulfide bonds
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additional information
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sperm surface protein disulfide isomerase activity plays a role in gamete fusion and sperm-egg interaction, the enzyme mediates conformational changes by thiol-disulfide exchange in fusion-active proteins, participation of ERp57, overview
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additional information
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the enzyme mediates conformational changes by thiol-disulfide exchange
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additional information
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PDI is required in vivo for both fibrin generation and platelet thrombus formation
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additional information
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protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
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additional information
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enzyme converts initiator protein tissue factor cysteine residues from glutathionylated to disulfide state
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AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
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additional information
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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a cysteine residue in the thioredoxin-like domain of AGR2 forms mixed disulfide bonds with MUC2, mutational analysis of the AGR2-MUC2 interaction, overview
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additional information
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the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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additional information
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PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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the enzyme is involved in the oxidative folding of cystine knot defense proteins and in in the biosynthesis of insecticidal cyclotides, overview, the Oldenlandia affinis plant accumulates knotted circular proteins called cyclotides
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additional information
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PDI interacts with the cyclotide precursor protein Oak1, PDi is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, properties of disulfide species, overview
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additional information
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PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme shows disulfide oxidase/isomerase, reductase, and chaperone activities, overview
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contains two CGHC active sites within two thioredoxin domains
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additional information
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the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contains two CGHC active sites within two thioredoxin domains
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additional information
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isoform PDI-A shows no activity with insulin, NADPH thioredoxin reductase , NADP malate dehydrogenase, peroxiredoxin, or RNase A
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additional information
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DsbA and DsbC are involved in disulfide bond formation and play an important role in the formation of extracellular enzymes, DsbA is important in lipase stability and excretion
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additional information
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the enzyme catalyzes dithiol-disulfide exchange reactions with an essential -C-P-Y-C- active site motif with catalytic C35 and C146, enzyme shows oxidative, reductive, and isomerase activities as well as ATPase activity, the latter being related to the enzyme's chaperone function
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additional information
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PDI has dehydroascorbate reductase activity
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additional information
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PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
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additional information
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modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
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additional information
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PDI is a multifunctional protein that is critically involved in the folding, assembly, and shedding of many cellular proteins via its isomerase activity in addition to being considered to function as an intracellular hormone reservoir
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additional information
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the enzyme shows hormone binding activity, e.g. of L-T3 and 17beta-estradiol hormones
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additional information
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PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold
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additional information
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PDI is a catalyst of isomerization of substrate protein intra- and extramolecular disulfide bridges and also has 3,3',5-triiodo-L-thyronine-binding activity and molecular chaperone-like activity
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additional information
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines
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additional information
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ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
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additional information
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ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
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additional information
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oxidative refolding of redRNaseA by disulfide isomerization activity, suppression of the thermal aggregation of alcohol dehydrogenase by chaperone activity, binding activity of 3,3',5-triiodo-L-thyronine in GH3 cells
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additional information
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the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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additional information
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the enzyme has an essential role that is distinct from its function in formation of native disulphides
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additional information
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essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
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additional information
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PDI plays a key role in catalyzing the folding of secretory proteins
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additional information
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regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
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additional information
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the organism is completely dependent on PDI activity for growth
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additional information
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all 5 domains of PDI are required for full catalytic activity
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additional information
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Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI
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additional information
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non-active site cysteines form a disulfide bridges which destabilizes the N-terminal active site disulfide rendering it a 18fold better oxidant by this way
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additional information
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the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
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additional information
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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additional information
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PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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additional information
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protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds
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additional information
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interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
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additional information
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PDI first recognizes the C-terminal domain of Mnl1p containing Asp607, Glu627, and Trp636 , PDI forms an intermolecular disulfide bond with C5 or C6 of Mnl1p. PDI introduces a disulfide bond between C1 and C3 in the MHDof Mnl1p, the disulfide bond between C1 and C3 in turn stabilizes association of PDI with Mnl1p, and the intermolecular disulfide bond between PDI and C5 or C6 of Mnl1p is partially reduced,whereas maintaining association of PDI and Mnl1p
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additional information
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the organism is completely dependent on PDI activity for growth
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additional information
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the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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additional information
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both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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additional information
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PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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additional information
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PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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the isozymes catalyze refolding of reduced and denatured lysozyme
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additional information
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the isozymes catalyze refolding of reduced and denatured lysozyme
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the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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the single domain PDI-1 and the class 1 PDI-2 of the organism both posses isomerase activity, but only the single domain PDI has reducing activity
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additional information
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the single domain PDI-1 and the class 1 PDI-2 of the organism both posses isomerase activity, but only the single domain PDI has reducing activity
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